Proteins containing the UBA domain are able to bind to multi-ubiquitin chains

The UBA domain is a motif found in a variety of proteins, some of which are associated with the ubiquitin–proteasome system. We describe the isolation of a fission-yeast gene, mud1+, which encodes a UBA domain containing protein that is able to bind multi-ubiquitin chains. We show that the UBA domain is responsible for this activity. Two other proteins containing this motif, the fission-yeast homologues of Rad23 and Dsk2, are also shown to bind multi-ubiquitin chains via their UBA domains. These two proteins are implicated, along with the fission-yeast Pus1(S5a/Rpn10) subunit of the 26 S proteasome, in the recognition and turnover of substrates by this proteolytic complex.

[1]  M. Lombaerts,et al.  Identification and characterization of the rhp23(+) DNA repair gene in Schizosaccharomyces pombe. , 2000, Biochemical and biophysical research communications.

[2]  M. Jones,et al.  Mph1, a member of the Mps1-like family of dual specificity protein kinases, is required for the spindle checkpoint in S. pombe. , 1998, Journal of cell science.

[3]  M. Glickman,et al.  The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover , 1996, Molecular and cellular biology.

[4]  S. Biggins,et al.  Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center , 1996, The Journal of cell biology.

[5]  Colin Gordon,et al.  Ubiquitin pathway: Another link in the polyubiquitin chain? , 1999, Current Biology.

[6]  C. Gordon,et al.  A Conditional Lethal Mutant in the Fission Yeast 26 S Protease Subunit mts3 Is Defective in Metaphase to Anaphase Transition (*) , 1996, The Journal of Biological Chemistry.

[7]  P. Philippsen,et al.  Heterologous modules for efficient and versatile PCR‐based gene targeting in Schizosaccharomyces pombe , 1998, Yeast.

[8]  Q. Deveraux,et al.  Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[9]  P. Bucher,et al.  The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. , 1996, Trends in biochemical sciences.

[10]  A. Udvardy,et al.  Cloning and sequencing a non-ATPase subunit of the regulatory complex of the Drosophila 26S protease. , 1995, European journal of biochemistry.

[11]  W. Baumeister,et al.  The 26S proteasome: a molecular machine designed for controlled proteolysis. , 1999, Annual review of biochemistry.

[12]  J. Benito,et al.  Regulation of the G1 phase of the cell cycle by periodic stabilization and degradation of the p25rum1 CDK inhibitor , 1998, The EMBO journal.

[13]  Q. Deveraux,et al.  Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[14]  Q. Deveraux,et al.  A 26 S protease subunit that binds ubiquitin conjugates. , 1994, The Journal of biological chemistry.

[15]  Li Chen,et al.  Rad23 links DNA repair to the ubiquitin/proteasome pathway , 1998, Nature.

[16]  K. Ferrell,et al.  Analysis of a Gene Encoding Rpn10 of the Fission Yeast Proteasome Reveals That the Polyubiquitin-binding Site of This Subunit Is Essential When Rpn12/Mts3 Activity Is Compromised* , 2000, The Journal of Biological Chemistry.

[17]  D. J. Clarke,et al.  UBA domains of DNA damage-inducible proteins interact with ubiquitin , 2001, Nature Structural Biology.

[18]  M. Seeger,et al.  Mts4, a Non-ATPase Subunit of the 26 S Protease in Fission Yeast Is Essential for Mitosis and Interacts Directly with the ATPase Subunit Mts2* , 1997, The Journal of Biological Chemistry.

[19]  A. Ciechanover,et al.  The ubiquitin system. , 1998, Annual review of biochemistry.